A team has used neutron crystallography to image all of the atoms in a radical intermediate of a copper amine oxidase enzyme. They disclosed previously unknown details, such as precise conformational changes, that help to explain the enzyme's biochemistry. This work might help researchers engineer enzymes that facilitate unusual chemistry or are highly efficient at room temperature that are useful in chemical industry.
When your wounds heal and your liver detoxifies a poison such as histamine you ingested, you can thank the class of enzymes known as copper amine oxidases for their assistance. Identifying the exact positions of the smallest hydrogen atoms in these enzymes is challenging with commonly used technologies, but is critical to engineering improved enzymes that exhibit unusual yet useful biochemical reactivity.
"There are pH-dependence, conformational change, and radical intermediate stabilization questions of our enzyme that X-ray crystallography in itself cannot fully explain," explains Takeshi Murakawa, lead author of the study."Neutron crystallography is well-suited for answering these questions."
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